DB code: S00297

RLCP classification	3.105.250000.48 : Transfer
CATH domain	3.40.50.270 : Rossmann fold	Catalytic domain
E.C.	2.7.1.69
CSA
M-CSA
MACiE

CATH domain	Related DB codes (homologues)
3.40.50.270 : Rossmann fold	S00298

Uniprot Enzyme Name
UniprotKB	Protein name	Synonyms	RefSeq	Pfam
P69795	N,N''-diacetylchitobiose-specific phosphotransferase enzyme IIB component	EC 2.7.1.69 PTS system N,N''-diacetylchitobiose-specific EIIB component	NP_416252.1 (Protein) NC_000913.2 (DNA/RNA sequence) YP_489999.1 (Protein) NC_007779.1 (DNA/RNA sequence)	PF02302 (PTS_IIB) [Graphical View]

KEGG enzyme name
protein-Npi-phosphohistidine---sugar phosphotransferase glucose permease PTS permease phosphotransferase, phosphohistidinoprotein-hexose enzyme IIl4ac gene glC proteins gene bglC RNA formation factors PEP-dependent phosphotransferase enzyme II PEP-sugar phosphotransferase enzyme II phosphoenolpyruvate-sugar phosphotransferase enzyme II phosphohistidinoprotein-hexose phosphotransferase phosphohistidinoprotein-hexose phosphoribosyltransferase phosphoprotein factor-hexose phosophotransferase protein, specific or class, gene bglC ribonucleic acid formation factor, gene glC sucrose phosphotransferase system II protein-Npi-phosphohistidine:sugar N-pros-phosphotransferase protein-Npi-phosphohistidine:sugar Npi-phosphotransferase

KEGG enzyme name

protein-Npi-phosphohistidine---sugar phosphotransferase
glucose permease
PTS permease
phosphotransferase, phosphohistidinoprotein-hexose
enzyme IIl4ac
gene glC proteins
gene bglC RNA formation factors
PEP-dependent phosphotransferase enzyme II
PEP-sugar phosphotransferase enzyme II
phosphoenolpyruvate-sugar phosphotransferase enzyme II
phosphohistidinoprotein-hexose phosphotransferase
phosphohistidinoprotein-hexose phosphoribosyltransferase
phosphoprotein factor-hexose phosophotransferase
protein, specific or class, gene bglC
ribonucleic acid formation factor, gene glC
sucrose phosphotransferase system II
protein-Npi-phosphohistidine:sugar N-pros-phosphotransferase
protein-Npi-phosphohistidine:sugar Npi-phosphotransferase

UniprotKB: Accession Number	Entry name	Activity	Subunit	Subcellular location	Cofactor
P69795	PTQB_ECOLI	Protein EIIB N(pi)-phospho-L- histidine/cysteine + sugar = protein EIIB + sugar phosphate.	Monomer, in both its unphosphorylated and phosphorylated forms.	Cytoplasm.

KEGG Pathways
Map code	Pathways	E.C.
MAP00010	Glycolysis / Gluconeogenesis
MAP00051	Fructose and mannose metabolism
MAP00052	Galactose metabolism
MAP00053	Ascorbate and aldarate metabolism
MAP00500	Starch and sucrose metabolism
MAP00530	Aminosugars metabolism

Compound table
	Substrates		Products		Intermediates
KEGG-id	C04261	C11477	C00615	C00934
E.C.
Compound	Protein N(pi)-phospho-L-histidine	Sugar	Protein histidine	Sugar phosphate
Type	aromatic ring (with nitrogen atoms),peptide/protein,phosphate group/phosphate ion	polysaccharide	aromatic ring (with nitrogen atoms),peptide/protein	phosphate group/phosphate ion,polysaccharide
ChEBI
PubChem

1e2bA	Unbound	Unbound	Unbound	Unbound
1iibA	Unbound	Unbound	Unbound	Unbound
1iibB	Unbound	Unbound	Unbound	Unbound
1h9cA	Unbound	Unbound	Unbound	Unbound

Reference for Active-site residues
resource	references	E.C.
Swiss-prot,Phosphorylation site

Active-site residues
PDB	Catalytic residues	Cofactor-binding residues	Modified residues	Main-chain involved in catalysis	Comment

1e2bA					mutant C10S
1iibA					mutant C10S
1iibB					mutant C10S
1h9cA	CSP 10		CSP 10 (phosphorylated cys)		phosphorylation site

References for Catalytic Mechanism
References	Sections	No. of steps in catalysis
[4]	p.221-222

References
[1]
Resource
Comments
Medline ID
PubMed ID	2092358
Journal	Res Microbiol
Year	1990
Volume	141
Pages	1061-7
Authors	Reizer J, Reizer A, Saier MH Jr
Title	The cellobiose permease of Escherichia coli consists of three proteins and is homologous to the lactose permease of Staphylococcus aureus.
Related PDB
Related UniProtKB	P69795
[2]
Resource
Comments
Medline ID
PubMed ID	8003964
Journal	Protein Sci
Year	1994
Volume	3
Pages	282-90
Authors	Ab E, Schuurman-Wolters GK, Saier MH, Reizer J, Jacuinod M, Roepstorff P, Dijkstra K, Scheek RM, Robillard GT
Title	Enzyme IIBcellobiose of the phosphoenol-pyruvate-dependent phosphotransferase system of Escherichia coli: backbone assignment and secondary structure determined by three-dimensional NMR spectroscopy.
Related PDB
Related UniProtKB	P69795
[3]
Resource
Comments
Medline ID
PubMed ID	9041631
Journal	Protein Sci
Year	1997
Volume	6
Pages	304-14
Authors	Ab E, Schuurman-Wolters G, Reizer J, Saier MH, Dijkstra K, Scheek RM, Robillard GT
Title	The NMR side-chain assignments and solution structure of enzyme IIBcellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli.
Related PDB	1e2b
Related UniProtKB	P69795
[4]
Resource
Comments
Medline ID
PubMed ID	9032081
Journal	Structure
Year	1997
Volume	5
Pages	217-25
Authors	van Montfort RL, Pijning T, Kalk KH, Reizer J, Saier MH Jr, Thunnissen MM, Robillard GT, Dijkstra BW
Title	The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases.
Related PDB	1iib
Related UniProtKB	P69795

Comments
The same E.C. number (2.7.1.69) appears in D00527, D00525, S00283, S00420, S00046. All of them are enzymes in PTS system. In the phosphotransferase (PTS) system, a phosphoryl group is transferred from phosphoenolpyruvate (PEP) via the PTS enzymes, EI, HPr, IIA, IIB to the tranported sugar. The enzyme here is IIB subunit of a cellobiose transporter (IIB-cellobiose). The transfer of the phosphoryl group proceeds via an associative mechanism with a pentavalent phosphorus intermediate. Although positively charged residues are usually important for the stabilization of the negatively charged reaction intermediate, IIB-cellobiose lacks not only such residues but also any other positively charged residues. This suggests that in the phosphotransfer reactions between IIA-cellobiose and IIB-cellobiose, and between IIB-cellobiose and the translocated cellobiose, stabilization of the respective transition states is carried out by residues located on IIA-cellobiose and the membrane-bound IIC-cellobiose, respectively.

Comments

The same E.C. number (2.7.1.69) appears in D00527, D00525, S00283, S00420, S00046. All of them are enzymes in PTS system.
In the phosphotransferase (PTS) system, a phosphoryl group is transferred from phosphoenolpyruvate (PEP) via the PTS enzymes, EI, HPr, IIA, IIB to the tranported sugar. The enzyme here is IIB subunit of a cellobiose transporter (IIB-cellobiose).
The transfer of the phosphoryl group proceeds via an associative mechanism with a pentavalent phosphorus intermediate. Although positively charged residues are usually important for the stabilization of the negatively charged reaction intermediate, IIB-cellobiose lacks not only such residues but also any other positively charged residues. This suggests that in the phosphotransfer reactions between IIA-cellobiose and IIB-cellobiose, and between IIB-cellobiose and the translocated cellobiose, stabilization of the respective transition states is carried out by residues located on IIA-cellobiose and the membrane-bound IIC-cellobiose, respectively.

Created	Updated
2002-07-27	2009-03-04